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Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Structural and functional insights into O-methyltransferase from Bacillus cereus
Jang-Hee Cho1, Younghee Park, Joong-Hoon Ahn
1Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 151-921, Korea.
Journal of Molecular Biology
|August 19, 2008
Summary
Bacterial O-methyltransferases (OMTs) like BcOMT2 methylate flavonoids. Structural studies reveal Mg(2+)-dependent dimerization and substrate specificity mechanisms, aiding novel compound discovery.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Bacterial O-methyltransferases (OMTs) are less understood than other OMTs.
- Bacterial OMTs may catalyze reactions for novel compound synthesis.
Purpose of the Study:
- Investigate structural and functional characteristics of Bacillus cereus OMT2 (BcOMT2).
- Elucidate the mechanism of O-methylation, dimerization, and substrate specificity of BcOMT2.
Main Methods:
- X-ray crystallography to solve apoenzyme and SAH co-complex structures.
- Mutational analysis to confirm enzyme dependency.
- In vitro enzymatic assays for O-methylation activity.
Main Results:
- BcOMT2 is a dimeric enzyme with a unique N-terminal helical dimerization region.
- S-adenosylhomocysteine (SAH) binding stabilizes dimerization and orders substrate specificity determinants.
- BcOMT2 active site resembles metal-dependent OMTs; enzyme confirmed as Mg(2+)-dependent.
Conclusions:
- Structural insights into BcOMT2 dimerization and substrate specificity.
- Understanding of Mg(2+)-dependent O-methylation mechanism in bacteria.
- Potential for engineering BcOMT2 for novel compound production.
